ID   PEPT_STRPM              Reviewed;         407 AA.
AC   Q48U99;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Peptidase T {ECO:0000255|HAMAP-Rule:MF_00550};
DE            EC=3.4.11.4 {ECO:0000255|HAMAP-Rule:MF_00550};
DE   AltName: Full=Aminotripeptidase {ECO:0000255|HAMAP-Rule:MF_00550};
DE            Short=Tripeptidase {ECO:0000255|HAMAP-Rule:MF_00550};
DE   AltName: Full=Tripeptide aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00550};
GN   Name=pepT {ECO:0000255|HAMAP-Rule:MF_00550}; OrderedLocusNames=M28_Spy0593;
OS   Streptococcus pyogenes serotype M28 (strain MGAS6180).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=319701;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS6180;
RX   PubMed=16088825; DOI=10.1086/430618;
RA   Green N.M., Zhang S., Porcella S.F., Nagiec M.J., Barbian K.D., Beres S.B.,
RA   Lefebvre R.B., Musser J.M.;
RT   "Genome sequence of a serotype M28 strain of group A Streptococcus:
RT   potential new insights into puerperal sepsis and bacterial disease
RT   specificity.";
RL   J. Infect. Dis. 192:760-770(2005).
CC   -!- FUNCTION: Cleaves the N-terminal amino acid of tripeptides.
CC       {ECO:0000255|HAMAP-Rule:MF_00550}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of the N-terminal residue from a tripeptide.;
CC         EC=3.4.11.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00550};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00550};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00550};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00550}.
CC   -!- SIMILARITY: Belongs to the peptidase M20B family. {ECO:0000255|HAMAP-
CC       Rule:MF_00550}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAX71707.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000056; AAX71707.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_021340972.1; NC_007296.2.
DR   AlphaFoldDB; Q48U99; -.
DR   SMR; Q48U99; -.
DR   MEROPS; M20.003; -.
DR   EnsemblBacteria; AAX71707; AAX71707; M28_Spy0593.
DR   KEGG; spb:M28_Spy0593; -.
DR   HOGENOM; CLU_053676_0_0_9; -.
DR   Proteomes; UP000009292; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0045148; F:tripeptide aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043171; P:peptide catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00550; Aminopeptidase_M20; 1.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   InterPro; IPR010161; Peptidase_M20B.
DR   PANTHER; PTHR42994:SF1; PTHR42994:SF1; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF037215; Peptidase_M20B; 1.
DR   SUPFAM; SSF55031; SSF55031; 1.
DR   TIGRFAMs; TIGR01882; peptidase-T; 1.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Cytoplasm; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Zinc.
FT   CHAIN           1..407
FT                   /note="Peptidase T"
FT                   /id="PRO_0000185324"
FT   ACT_SITE        84
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT   ACT_SITE        177
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT   BINDING         82
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT   BINDING         143
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT   BINDING         143
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT   BINDING         178
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT   BINDING         200
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT   BINDING         382
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
SQ   SEQUENCE   407 AA;  44999 MW;  273711B4A6509CE2 CRC64;
     MKYDNLLDRF IKYVKVNTRS DPDSETTPST ESQEAFALTI LKPEMEAIGL QDVHYNPVNG
     YLIGTLPANN PTLTRKIGFI AHMDTADFNA ENVNPQIIDN YQGGDITLGS SNYKLDPKAF
     PNLNNYIGQT LITTDGTTLL GADDKSGIAE IMTAIEFLTS QPQIEHCDIK VAFGPDEEIG
     VGADKFEVAD FEVDFAYTMD GGPLGELQYE TFSAAALEVT FLGRNVHPGT AKDQMINALE
     LAIDFHEKLP AKERPEYTDG YQGFYHLTGL TGTVEEARAS YIIRDFEEAS FEARKVKVEN
     IAQSMNAQLG TKRVLVELND QYYNMKKVIE KDMTAIELAK EVMEELAIKP VIEPIRGGTD
     GSKISFMGIP TPNIFAGGEN MHGRFEFVSL QTMERAVDVI IGLVCKA